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Cell. 2006 Jan 27;124(2):355-66.

Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III.

Author information

1
Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.

Abstract

Members of the ribonuclease III (RNase III) family are double-stranded RNA (dsRNA) specific endoribonucleases characterized by a signature motif in their active centers and a two-base 3' overhang in their products. While Dicer, which produces small interfering RNAs, is currently the focus of intense interest, the structurally simpler bacterial RNase III serves as a paradigm for the entire family. Here, we present the crystal structure of an RNase III-product complex, the first catalytic complex observed for the family. A 7 residue linker within the protein facilitates induced fit in protein-RNA recognition. A pattern of protein-RNA interactions, defined by four RNA binding motifs in RNase III and three protein-interacting boxes in dsRNA, is responsible for substrate specificity, while conserved amino acid residues and divalent cations are responsible for scissile-bond cleavage. The structure reveals a wealth of information about the mechanism of RNA hydrolysis that can be extrapolated to other RNase III family members.

PMID:
16439209
DOI:
10.1016/j.cell.2005.11.034
[Indexed for MEDLINE]
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